1ix5
From Proteopedia
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| - | [[Image:1ix5.jpg|left|200px]]<br /><applet load="1ix5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ix5" /> | ||
| - | '''Solution structure of the Methanococcus thermolithotrophicus FKBP'''<br /> | ||
| - | == | + | ==Solution structure of the Methanococcus thermolithotrophicus FKBP== |
| + | <StructureSection load='1ix5' size='340' side='right'caption='[[1ix5]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ix5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus Methanothermococcus thermolithotrophicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IX5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ix5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix5 OCA], [https://pdbe.org/1ix5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ix5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ix5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ix5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FKBPS_METTL FKBPS_METTL] Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (PubMed:9440528, PubMed:10631007). Also exhibits chaperone-like activity (PubMed:10631007). In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates (PubMed:9440528, PubMed:10631007).<ref>PMID:10631007</ref> <ref>PMID:9440528</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ix5_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ix5 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity. | Here we report the solution structure of an archaeal FK506-binding protein (FKBP) from a thermophilic archaeum, Methanococcus thermolithotrophicus (MtFKBP17), which has peptidyl prolyl cis-trans isomerase (PPIase) and chaperone-like activities, to reveal the structural basis for the dual function. In addition to a typical PPIase domain, a newly identified domain is formed in the flap loop by a 48-residue insert that is required for the chaperone-like activity. The new domain, called IF domain (the Insert in the Flap), is a novel-folding motif and exposes a hydrophobic surface, which we consider to play an important role in the chaperone-like activity. | ||
| - | + | Three-dimensional solution structure of an archaeal FKBP with a dual function of peptidyl prolyl cis-trans isomerase and chaperone-like activities.,Suzuki R, Nagata K, Yumoto F, Kawakami M, Nemoto N, Furutani M, Adachi K, Maruyama T, Tanokura M J Mol Biol. 2003 May 16;328(5):1149-60. PMID:12729748<ref>PMID:12729748</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1ix5" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[FKBP 3D structures|FKBP 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanothermococcus thermolithotrophicus]] | ||
| + | [[Category: Adachi K]] | ||
| + | [[Category: Furutani M]] | ||
| + | [[Category: Kawakami M]] | ||
| + | [[Category: Maruyama T]] | ||
| + | [[Category: Nagata K]] | ||
| + | [[Category: Nemoto N]] | ||
| + | [[Category: Suzuki R]] | ||
| + | [[Category: Tanokura M]] | ||
Current revision
Solution structure of the Methanococcus thermolithotrophicus FKBP
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